Proteomics

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A proteome-wide screen of Cdc14 interactors in Candida albicans


ABSTRACT: The Cdc14 phosphatase plays a key role in organising the intricate choreography of mitosis and cell division. In order to understand the role of Cdc14 in the human fungal pathogen Candida albicans we used quantitative proteomics to identify interacting proteins of CaCdc14. We used an orthogonal approach of a substrate trapping mutant combined with affinity purification-mass spectrometry analysis using stable isotope labelling in cell culture (SILAC). The results identified 126 proteins that interact with Cdc14 of which 80% are novel. These provide further insight into the function of Cdc14, highlighting roles in regulating the attachment of the mitotic spindle to kinetochores, mitotic exit, cytokinesis, licensing of DNA replication by re-activating pre-replication complexes, and DNA repair. Five Cdc14-interacting proteins with previously unknown functions localized to the Spindle Pole Bodies (SPBs). Intriguingly, there was suggestive evidence that Cdc14 substrates may include components of the ergosterol biosynthesis pathway targeted by azole anti-fungal drugs Thus we have greatly expanded the set of known substrates of Cdc14 by which it carries out these roles.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Candida Albicans (yeast)

TISSUE(S): Fungal Cell

SUBMITTER: Iliyana Kaneva  

LAB HEAD: Mark Dickman

PROVIDER: PXD009581 | Pride | 2019-11-12

REPOSITORIES: Pride

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Publications

Proteins that physically interact with the phosphatase Cdc14 in Candida albicans have diverse roles in the cell cycle.

Kaneva Iliyana N IN   Sudbery Ian M IM   Dickman Mark J MJ   Sudbery Peter E PE  

Scientific reports 20190418 1


The chromosome complement of the human fungal pathogen Candida albicans is unusually unstable, suggesting that the process of nuclear division is error prone. The Cdc14 phosphatase plays a key role in organising the intricate choreography of mitosis and cell division. In order to understand the role of Cdc14 in C. albicans we used quantitative proteomics to identify proteins that physically interact with Cdc14. To distinguish genuine Cdc14-interactors from proteins that bound non-specifically to  ...[more]

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